Reviewed,
UniProtKB/Swiss-Prot Q86W56 (PARG_HUMAN)
Last modified
October 13, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Poly(ADP-ribose) glycohydrolase EC=3.2.1.143 | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 976 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism may be required for maintenance of the normal function of neuronal cells. |
| Catalytic activity | Hydrolyzes poly(ADP-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-ribose. |
| Subcellular location | Isoform 1: Nucleus. Isoform 2: Cytoplasm. Isoform 3: Cytoplasm. |
| Tissue specificity | Ubiquitously expressed. Ref.1 |
| Sequence similarities | Belongs to the poly(ADP-ribose) glycohydrolase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Nucleus |
| Coding sequence diversity | Alternative splicing |
| Molecular function | Hydrolase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | poly(ADP-ribose) glycohydrolase activity Inferred from direct assay. Source: UniProtKB |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q86W56-1) Also known as: hPARG111; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q86W56-2) Also known as: hPARG102; The sequence of this isoform differs from the canonical sequence as follows: 1-82: Missing. | ||||||
| Isoform 3 (identifier: Q86W56-3) Also known as: hPARG99; The sequence of this isoform differs from the canonical sequence as follows: 1-108: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 976 | 976 | Poly(ADP-ribose) glycohydrolase | PRO_0000066602 | |||||
Regions | |||||||||
| Motif | 10 – 16 | 7 | Nuclear localization signal | ||||||
Amino acid modifications | |||||||||
| Modified residue | 133 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 137 | 1 | Phosphoserine Ref.8 Ref.7 | ||||||
| Modified residue | 139 | 1 | Phosphothreonine Ref.7 | ||||||
| Modified residue | 197 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 199 | 1 | Phosphothreonine Ref.8 | ||||||
| Modified residue | 261 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 264 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 316 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 503 | 1 | N6-acetyllysine Ref.10 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 108 | 108 | Missing in isoform 3. | VSP_011770 | |||||
| Alternative sequence | 1 – 82 | 82 | Missing in isoform 2. | VSP_011769 | |||||
Experimental info | |||||||||
| Mutagenesis | 12 | 1 | K → A: Abolishes nuclear targeting; when associated with G-13. Ref.2 | ||||||
| Mutagenesis | 13 | 1 | R → G: Abolishes nuclear targeting; when associated with A-12. Ref.2 | ||||||
| Mutagenesis | 36 | 1 | R → A: No effect. Ref.2 | ||||||
| Mutagenesis | 37 | 1 | R → G: No effect. Ref.2 | ||||||
| Sequence conflict | 13 – 14 | 2 | RP → AT in AAB61614. Ref.3 | ||||||
| Sequence conflict | 61 | 1 | R → Q in AAB61614. Ref.3 | ||||||
| Sequence conflict | 127 | 1 | E → V in AAB61614. Ref.3 | ||||||
| Sequence conflict | 138 | 1 | P → L in AAB61614. Ref.3 | ||||||
| Sequence conflict | 227 | 1 | Q → H in AAB61614. Ref.3 | ||||||
| Sequence conflict | 242 | 1 | D → H in AAB61614. Ref.3 | ||||||
| Sequence conflict | 260 | 1 | E → K in AAB61614. Ref.3 | ||||||
| Sequence conflict | 275 | 1 | P → S in AAB61614. Ref.3 | ||||||
| Sequence conflict | 282 | 1 | T → I in AAB61614. Ref.3 | ||||||
| Sequence conflict | 414 | 1 | F → L in AAB61614. Ref.3 | ||||||
| Sequence conflict | 814 – 815 | 2 | WQ → CE in AAB61614. Ref.3 | ||||||
| Sequence conflict | 817 | 1 | R → H in AAH52966. Ref.5 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Human poly(ADP-ribose) glycohydrolase (PARG) gene and the common promoter sequence it shares with inner mitochondrial membrane translocase 23 (TIM23)." Meyer R.G., Meyer-Ficca M.L., Jacobson E.L., Jacobson M.K. Gene 314:181-190(2003) [PubMed: 14527731] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Skin. |
| [2] | "Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments." Meyer-Ficca M.L., Meyer R.G., Coyle D.L., Jacobson E.L., Jacobson M.K. Exp. Cell Res. 297:521-532(2004) [PubMed: 15212953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), MUTAGENESIS OF LYS-12; ARG-13; ARG-36 AND ARG-37. Tissue: Skin. |
| [3] | "Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization." Ame J.-C., Apiou F., Jacobson E.L., Jacobson M.K. Cytogenet. Cell Genet. 85:269-270(1999) [PubMed: 10449915] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [4] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Brain cortex, Hippocampus and Testis. |
| [5] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin and Testis. |
| [6] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, MASS SPECTROMETRY. Tissue: Epithelium. |
| [7] | "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND THR-139, MASS SPECTROMETRY. |
| [8] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-137; SER-197 AND THR-199, MASS SPECTROMETRY. |
| [9] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [10] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-503, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AY258587 mRNA. Translation: AAP83314.1. AY575848 mRNA. Translation: AAT66421.1. AY575849 mRNA. Translation: AAT66422.1. AF005043 mRNA. Translation: AAB61614.1. AK295786 mRNA. Translation: BAG58607.1. AK302560 mRNA. Translation: BAG63826.1. AK314909 mRNA. Translation: BAG37421.1. BC050560 mRNA. Translation: AAH50560.1. BC052966 mRNA. Translation: AAH52966.1. | |
| IPI | IPI00470744. IPI00759749. IPI00787604. |
| RefSeq | NP_003622.2. |
| UniGene | Hs.535298 Hs.709578 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q86W56. |
PTM databases | |
| PhosphoSite | Q86W56. |
Proteomic databases | |
| PRIDE | Q86W56. |
Genome annotation databases | |
| Ensembl | ENST00000399369; ENSP00000382303; ENSG00000214982; Homo sapiens. [Genome view] ENST00000429875; ENSP00000412843; ENSG00000214982; Homo sapiens. [Genome view] ENST00000435772; ENSP00000396513; ENSG00000214982; Homo sapiens. [Genome view] |
| GeneID | 8505. |
| KEGG | hsa:8505. |
| UCSC | uc001jif.1. human. |
Organism-specific databases | |
| CTD | 8505. |
| GeneCards | GC10P051293. |
| HGNC | HGNC:8605. PARG. |
| HPA | HPA021819. |
| MIM | 603501. gene. |
| PharmGKB | PA32940. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | Q86W56. |
| HOVERGEN | Q86W56. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.143. 247. |
Gene expression databases | |
| ArrayExpress | Q86W56. |
| CleanEx | HS_PARG. |
| Genevestigator | Q86W56. |
| GermOnline | ENSG00000204155. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR007724. Poly_GlycHdrlase. [Graphical view] |
| PANTHER | PTHR12837. Poly_glchydro. 1 hit. |
| Pfam | PF05028. PARG_cat. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 31829. |
| PMAP-CutDB | Q86W56. |
| SOURCE | Search... |
Entry information
| Entry name | PARG_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q86W56 Secondary accession number(s): B2RC24 Q9Y4W7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| Human chromosome 10 Human chromosome 10: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


